title: The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity.
abstract: Protein arginine methylation is a common post-translational modification in eukaryotes that is catalyzed by a family of the protein arginine methyltransferases (PRMTs). PRMTs are classified into three types: type I and type II add asymmetrically and symmetrically dimethyl groups to arginine, respectively, while type III adds solely monomethyl group to arginine. However, although the enzymatic activity of type I and type II PRMTs have been reported, the substrate specificity and the methylation activity of type III PRMTs still remains unknown. Here, we report the characterization of Caenorhabditis elegans PRMT-2 and PRMT-3, both of which are highly homologous to human PRMT7. We find that these two PRMTs can bind to S-adenosyl methionine (SAM), but only PRMT-3 has methyltransferase activity for histone H2A depending on its SAM-binding domain. Importantly, thin-layer chromatographic analysis demonstrates that PRMT-3 catalyzes the formation of monomethylated, but not dimethylated arginine. Our study thus identifies the first type III PRMT in C. elegans and provides a means to elucidate the physiological significance of arginine monomethylation in multicellular organisms.
authors.affiliation: The Life Science Center, Tsukuba Advanced Research Alliance, Graduate School of Life and Environmental Sciences,University of Tsukuba, Tsukuba, Ibaraki, Japan.
authors.forename: Yuta
authors.initials: Y
authors.lastname: Takahashi
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Daitoku
authors.forename: Atsuko
authors.initials: A
authors.lastname: Yokoyama
authors.forename: Kimihiro
authors.initials: K
authors.lastname: Nakayama
authors.forename: Jun-Dal
authors.initials: JD
authors.lastname: Kim
authors.forename: Akiyoshi
authors.initials: A
authors.lastname: Fukamizu
mesh_terms: D000818:Animals; D055162:Biocatalysis; D017173:Caenorhabditis elegans / Q000201:enzymology*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000378:metabolism; D006801:Humans; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry; D010802:Phylogeny; D011485:Protein Binding; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics / Q000378:metabolism*; D012436:S-Adenosylmethionine / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D019323:omega-N-Methylarginine / Q000378:metabolism
chemical_list: D029742:Caenorhabditis elegans Proteins; D006657:Histones; D019323:omega-N-Methylarginine; D012436:S-Adenosylmethionine; D008780:Methyltransferases; C487994:PRMT7 protein, human; D011484:Protein-Arginine N-Methyltransferases